Catalytic properties of lysyl hydroxylase from cells synthesizing genetically different collagen types.
Crude preparations of lysyl hydroxylase were extracted from chick-embryo tendons synthesizing exclusively type I collagen, chick-embryo sterna synthesizing exclusively type II collagen and HT-1080 sarcoma cells synthesizing exclusively type IV collagen. No differences were found in the Km values for Fe2+, 2-oxoglutarate and ascorbate between these three enzymes preparations. Similarly no differences were found in the Km values for type I and type II protocollagens and the rate at which type IV protocollagen is hydroxylated between these enzyme preparations. The extent to which type I protocollagen could be hydroxylated by the three enzymes was likewise identical. These data strongly argue against the existence of collagen-type-specific lysyl hydroxylase isoenzymes.
D000818:Animals; D002460:Cell Line; D002642:Chick Embryo; D003094:Collagen / Q000096:biosynthesis* / Q000235:genetics; D006801:Humans; D007527:Isoenzymes / Q000378:metabolism*; D007700:Kinetics; D006899:Mixed Function Oxygenases / Q000378:metabolism*; D011347:Procollagen / Q000378:metabolism; D008240:Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase / Q000378:metabolism*; D012509:Sarcoma / Q000201:enzymology; D013249:Sternum / Q000201:enzymology; D013710:Tendons / Q000201:enzymology
D007527:Isoenzymes; D011347:Procollagen; D003094:Collagen; D006899:Mixed Function Oxygenases; D008240:Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase